ID MY18A_RAT Reviewed; 2044 AA.
AC D3ZFD0;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 24-JAN-2024, entry version 91.
DE RecName: Full=Unconventional myosin-XVIIIa {ECO:0000305};
GN Name=Myo18a {ECO:0000312|RGD:1562698};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=31522887; DOI=10.1016/j.cell.2019.08.025;
RA Fu M.M., McAlear T.S., Nguyen H., Oses-Prieto J.A., Valenzuela A.,
RA Shi R.D., Perrino J.J., Huang T.T., Burlingame A.L., Bechstedt S.,
RA Barres B.A.;
RT "The Golgi outpost protein TPPP nucleates microtubules and is critical for
RT myelination.";
RL Cell 0:0-0(2019).
CC -!- FUNCTION: May link Golgi membranes to the cytoskeleton and participate
CC in the tensile force required for vesicle budding from the Golgi.
CC Thereby, may play a role in Golgi membrane trafficking and could
CC indirectly give its flattened shape to the Golgi apparatus.
CC Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BPB, has been
CC involved in modulating lamellar actomyosin retrograde flow that is
CC crucial to cell protrusion and migration (By similarity). May be
CC involved in the maintenance of the stromal cell architectures required
CC for cell to cell contact (By similarity). Regulates trafficking,
CC expression, and activation of innate immune receptors on macrophages.
CC Plays a role to suppress inflammatory responsiveness of macrophages via
CC a mechanism that modulates CD14 trafficking. Acts as a receptor of
CC surfactant-associated protein A (SFTPA1/SP-A) and plays an important
CC role in internalization and clearance of SFTPA1-opsonized S.aureus by
CC alveolar macrophages. Strongly enhances natural killer cell
CC cytotoxicity (By similarity). {ECO:0000250|UniProtKB:Q92614,
CC ECO:0000250|UniProtKB:Q9JMH9}.
CC -!- SUBUNIT: Homodimer. Forms a tripartite complex with CDC42BPA/CDC42BPB
CC and LURAP1 with the latter acting as an adapter connecting
CC CDC42BPA/CDC42BPB and MYO18A. Binds F-actin; regulated by ADP and
CC GOLPH3. Interacts with GOLPH3; the interaction is direct and may link
CC Golgi membranes to the actin cytoskeleton. Interacts with JAK3.
CC Interacts with MSR1 and CD14. {ECO:0000250|UniProtKB:Q92614}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q92614}.
CC Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q92614}.
CC Golgi outpost {ECO:0000269|PubMed:31522887}. Cytoplasm, cytoskeleton,
CC microtubule organizing center {ECO:0000269|PubMed:31522887}.
CC Note=Recruited to the Golgi apparatus by GOLPH3 (By similarity).
CC Localizes to the postsynaptic Golgi apparatus region, also named Golgi
CC outpost, which shapes dendrite morphology by functioning as sites of
CC acentrosomal microtubule nucleation (PubMed:31522887).
CC {ECO:0000250|UniProtKB:Q92614, ECO:0000269|PubMed:31522887}.
CC -!- DOMAIN: The myosin motor domain binds ADP and ATP but has no intrinsic
CC ATPase activity. Mediates ADP-dependent binding to actin.
CC {ECO:0000250|UniProtKB:Q92614}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; AABR07030054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07030055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; D3ZFD0; -.
DR SMR; D3ZFD0; -.
DR STRING; 10116.ENSRNOP00000070473; -.
DR PhosphoSitePlus; D3ZFD0; -.
DR jPOST; D3ZFD0; -.
DR PaxDb; 10116-ENSRNOP00000050980; -.
DR PeptideAtlas; D3ZFD0; -.
DR AGR; RGD:1562698; -.
DR RGD; 1562698; Myo18a.
DR VEuPathDB; HostDB:ENSRNOG00000033101; -.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; D3ZFD0; -.
DR PRO; PR:D3ZFD0; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000033101; Expressed in skeletal muscle tissue and 19 other cell types or tissues.
DR ExpressionAtlas; D3ZFD0; baseline and differential.
DR GO; GO:0042641; C:actomyosin; ISO:RGD.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:GOC.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0043531; F:ADP binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0031032; P:actomyosin structure organization; ISO:RGD.
DR GO; GO:0090164; P:asymmetric Golgi ribbon formation; ISO:RGD.
DR GO; GO:0007249; P:canonical NF-kappaB signal transduction; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0071346; P:cellular response to type II interferon; ISO:RGD.
DR GO; GO:0007030; P:Golgi organization; ISO:RGD.
DR GO; GO:0090161; P:Golgi ribbon formation; ISO:RGD.
DR GO; GO:0048194; P:Golgi vesicle budding; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:1903028; P:positive regulation of opsonization; ISO:RGD.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:RGD.
DR GO; GO:0043030; P:regulation of macrophage activation; ISO:RGD.
DR CDD; cd01386; MYSc_Myo18; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.70.1590; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 4.10.270.10; Myosin, subunit A; 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR036064; MYSc_Myo18.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF13; UNCONVENTIONAL MYOSIN-XVIIIA; 1.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR Pfam; PF00595; PDZ; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Golgi apparatus; Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..2044
FT /note="Unconventional myosin-XVIIIa"
FT /id="PRO_0000448595"
FT DOMAIN 349..401
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 405..1175
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 1178..1207
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..398
FT /note="Mediates nucleotide-independent binding to F-actin
FT and interaction with GOLPH3"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1070
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 1045..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1840..1891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1950..2044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1239..1959
FT /evidence="ECO:0000255"
FT COMPBIAS 140..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1950..1975
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1989..2004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2006..2021
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2024..2044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 498..505
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 99
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 1057
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 1058
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 1060
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 1630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 1932
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 1960
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
FT MOD_RES 1964
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 1988
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
FT MOD_RES 1992
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 1996
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 1997
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 2010
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
FT MOD_RES 2026
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
FT MOD_RES 2031
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
FT MOD_RES 2033
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
FT MOD_RES 2035
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
SQ SEQUENCE 2044 AA; 232667 MW; B10E1FFD55D081CE CRC64;
MFNLMKKDKD KDGGRKEKKE KKEKKERMSA AELRSLEEMS MRRGFFNLNR SSKRESKTRL
EISNPIPIKV ASGSDLHLTD IDSDSNRGSI ILDSGHLSTA SSSDDLKGEE GSFRGSVLQR
AAKFGSLAKQ NSQMIVKRFS FSQRSRDESA SETSTPSEHS AAPSPQVEVR TLEGQLMQHS
GLGIPRPGPR SRVPELVTKR FPADLRLPAL VPPPPPALRE LELQRRPTGD FGFSLRRTTM
LDRAPEGQAY RRVVHFAEPG AGTKDLALGL VPGDRLVEIN GQNVENKSRD EIVEMIRQSG
DSVRLKVQPI PELSELSRSW LRTGEGHRRE PTDAKTEEQI AAEEAWYETE KVWLVHRDGF
SLASQLKSEE LSLPEGKVRV KLDHDGAILD VDEDDVEKAN APSCDRLEDL ASLVYLNESS
VLHTLRQRYG ASLLHTYAGP SLLVLSPRGA PAVYSEKVMH MFKGCRREDM APHIYAVAQT
AYRAMLMSRQ DQSIVLLGSS GSGKTTSSQH LVQYLATIAG TSGNKVFSVE KWQALATLLE
AFGNSPTIMN GSATRFSQIL SLDFDQAGQV ASASVQTMLL EKLRVARRPA SEATFNVFYY
LLACGDSTLR TELHLNHLAE NNVFGIVPLS KPEEKQRAAQ QFSKLQTAMK VLAISPEEQK
ACWLILASIY HLGAAGATKA VFSCGRKQFA RHEWAQKAAY LLGCSLEELS SAIFKHQLKG
GTLQRSTSFR QGPEESGLGE GTGTKLSALE CLEGMASGLY SELFTLLISL VNRALKSSQH
SLCSMMIVDT PGFQNPEWGG SARGASFEEL CHNYAQDRLQ KLFHERTFLQ ELERYKEDNI
ELAFDDLEPV TDDSVAAVDQ ASHQSLVRSL AHADEARGLL WLLEEEALVP GATEDTLLDR
LFSYYGPQEG DKKGQSPLLR SSKPRHFLLG HSHGTNWVEY NVTGWLNYTK QNPATQNAPR
LLQDSQNSVV ECLPSKRKAL GSVLSSEKKK RKKKKKKKCP ESANSVAHTY SLSTQTLQVD
ALIDTIKRSK MHFVHCFLPV AEGWPGEPRS ASSRRVSSSS ELDLPPGDPC EAGLLQLDVS
LLRAQLRGSR LLDAIRMYRQ GYPDHMVFSE FRRRFDVLAP HLTKKHGRNY IMVDEKRAVE
ELLESLDLEK SSCCMGLSRV FFRAGTLARL EEQRDEETSR HLTLFQAACR GYLARQHFKK
RKIQDLAIRC VQKNIKKNKG VKDWPWWKLF TTVRPLIQVQ LSEEQIRNKD EEIQQLRNKL
EKVEKERNEL RLNSDRLETR ISELTSELTD ERNTGESASQ LLDAETAERL RTEKEMKELQ
TQYDALKKQM EAMDMEVMEA RLIRAAEING EVDDDDAGGE WRLKYERAVR EVDFTKKRLQ
QELEDKMEVE QQNRRQLERR LGDLQADSDE SQRALQQLKK KCQRLTAELQ DTKLHLEGQQ
VRNHELEKKQ RRFDSELSQA HEETQREKLQ REKLQREKDM LLAEAFSLKQ QMEEKDLDIA
GFTQKVVSLE AELQDISSQE SKDEASLAKV KKQLRDLEAK VKDQEEELDE QAGSIQMLEQ
AKLRLEMEME RMRQTHSKEM ESRDEEVEEA RQSCQKKLRQ MEVQLEEEYE DKQKALREKR
ELESKLSTLS DQVNQRDFES EKRLRKDLKR TKALLADAQI MLDHLKNNAP SKREIAQLKN
QLEESEFTCA AAVKARKAME VEMEDLHLQI DDIAKAKTAL EEQLSRLQRE KNEIQNRLEE
DQEDMNELMK KHKAAVAQAS RDMAQMNDLQ AQLEESNKEK QELQEKLQAL QSQVEFLEQS
MVDKSLVSRQ EAKIRELETR LEFEKTQVKR LESMASRLKE NMEKLTEERD QRAAAENREK
EQNKRLQRQL RDTKEEMSEL ARKEAEASRK KHELEMDLES LEAANQSLQA DLKLAFKRIG
DLQAAIEDEM ESDENEDLIN SLQDMVTKYQ KRKNKLEGDS DVDSELEDRV DGVKSWLSKN
KGPSKAPSDD GSLKSSSPTS HWKSLAPDLS DDEHDPVDSI SRPRFSHNYL SDSDTEAKLT
ETNA
//
